By utilizing DEAE-Sephadex column chromatography in conjunction with specific affinity columns, it is possible to separate and purify a number of chromatin-associated protein kinases and phosphatases. These enzymes demonstrate multiplicity and some tissue specificity. Present studies are directed toward characterizing and quantitating these enzymes in rat ventral prostate nucleus, and this represents an initial step to studying the control exerted by androgen on these enzymes. It is also proposed to examine these activities in human prostatic tissue to determine if they are influenced by neoplasia. In studies of phosphorylation of chromosomal proteins, it appears that endogenous chromatin-associated protein kinase activity is capable of phosphorylating some of the high mobility group nonhistone proteins. Further work is proposed to study this reaction and its relation to androgen-mediated genome activation. Nuclear membrane has been shown to contain distinct protein kinase and phosphatase activities. Work is being undertaken to characterize these activities in the prostatic nuclear membrane.